Interactions of Rabconnectin-3 with Cav2 calcium channels.

This study describes the interaction between Cav2 calcium channels and Rabconnectin-3, a di-subunit protein that is associated with synaptic vesicles. Immunostaining reveals that both Rabconnectin-3? (RB-3?) and Rabconnectin-3? (RB-3?) are colocalized in mouse hippocampal neurons. Co-immunoprecipitations from brain tissue is consistent with the formation of a protein complex between RB-3? ...
and RB-3? and both Cav2.2 and the related Cav2.1 calcium channel. The coexpression of either RB-3? or RB-3? with Cav2.2 calcium channels in tsA-201 cells led to a reduction in Cav2.2 current density without any effects on the voltage-dependence of activation or inactivation. Coexpression of both Rabconnectin-3 subunits did not cause an additive effect on current densities. Finally, the presence of Rabconnectin-3 did not interfere with ?-opioid receptor mediated G?? modulation of Cav2.2 channels. Altogether, our findings show that Rabconnectin-3 has the propensity to regulate calcium entry mediated by Cav2.2 channels.
Mesh Terms:
Animals, Caveolin 2, GTP-Binding Proteins, Hippocampus, Humans, Mice, Nerve Tissue Proteins, Neurons, Protein Binding, Rats
Mol Brain
Date: Dec. 28, 2018
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